Journal
SCIENCE
Volume 375, Issue 6586, Pages 1281-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.abm5320
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Funding
- NIH [R35GM128661]
- Natural Science Engineering Research Council
- Canadian Institutes of Health Research [PJG-47391S]
- Ontario Graduate Scholarship
- University of Ottawa Excellence Scholarship
- Yale University Brown Fellowship
- Fonds de Recherche du Quebec-Nature et Technologies (FRQNT) [272565]
- University of Ottawa Heart Institute
- Wellcome Trust [104175/Z/14/Z, 203149]
- UK Biotechnology and Biological Sciences Research Council [BBS/E/B/000C0421]
- NSERCRTI [RTI-2019-00009]
- Wellcome Trust [104175/Z/14/Z] Funding Source: Wellcome Trust
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This study reveals the specific function of H3.1 during replication in plants, demonstrating its interaction with TSK and DNA polymerase theta in the absence of H3 lysine 27 monomethylation catalyzed by ATXR5/ATXR6. It also highlights a common strategy used in multicellular eukaryotes for regulating post-replicative chromatin maturation and the recognition of H3.1 variant by histone monomethyltransferases.
The tail of replication-dependent histone H3.1 varies from that of replication-independent H3.3 at the amino acid located at position 31 in plants and animals, but no function has been assigned to this residue to demonstrate a unique and conserved role for H3.1 during replication. We found that TONSOKU (TSK/TONSL), which rescues broken replication forks, specifically interacts with H3.1 via recognition of alanine 31 by its tetratricopeptide repeat domain. Our results indicate that genomic instability in the absence of ATXR5/ATXR6-catalyzed histone H3 lysine 27 monomethylation in plants depends on H3.1, TSK, and DNA polymerase theta (Pol theta). This work reveals an H3.1-specific function during replication and a common strategy used in multicellular eukaryotes for regulating post-replicative chromatin maturation and TSK, which relies on histone monomethyltransferases and reading of the H3.1 variant.
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